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Record 74 of 1139
A model of EcoRII restriction endonuclease action: the active complex is most likely formed by one protein subunit and one DNA recognition site
External Online Source: doi:10.1080/152165499307477
Author and Affiliation:
Karpova, E. A.(Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Science, Moscow Region)
Kubareva, E. A.
Shabarova, Z. A.
Abstract: To elucidate the mechanism of interaction of restriction endonuclease EcoRII with DNA, we studied by native gel electrophoresis the binding of this endonuclease to a set of synthetic DNA-duplexes containing the modified or canonical recognition sequence 5'-d(CCA/TGG)-3'. All binding substrate or substrate analogues tested could be divided into two major groups: (i) duplexes that, at the interaction with endonuclease EcoRII, form two types of stable complexes on native gel in the absence of Mg2+ cofactor; (ii) duplexes that form only one type of complex, observed both in the presence and absence of Mg2+. Unlike the latter, duplexes under the first group can be hydrolyzed by endonuclease. Data obtained suggest that the active complex is most likely formed by one protein subunit and one DNA recognition sequence. A model of EcoRII endonuclease action is presented.
Publication Date: Jul 01, 1999
Document ID:
20040141581
(Acquired Nov 09, 2004)
Subject Category: LIFE SCIENCES (GENERAL)
Document Type: Journal Article
Publication Information: IUBMB life (ISSN 1521-6543); Volume 48; 1; 91-8
Publisher Information: United Kingdom
Description: In English
Distribution Limits: Unclassified; Publicly available; Unlimited
Rights: Copyright
NASA Terms: DEOXYRIBONUCLEIC ACID; ENZYMES; POLYNUCLEOTIDES; PROTEINS; ACTIVE SITES (CHEMISTRY); MACROMOLECULES; MAGNESIUM; MODELS
Other Descriptors: DNA/CHEMISTRY/METABOLISM; DEOXYRIBONUCLEASES, TYPE II SITE-SPECIFIC/CHEMISTRY/METABOLISM; OLIGODEOXYRIBONUCLEOTIDES/CHEMISTRY/METABOLISM; BASE SEQUENCE; BINDING SITES; MACROMOLECULAR SYSTEMS; MAGNESIUM/CHEMISTRY; MODELS, THEORETICAL
Availability Source: Other Sources
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